Q8TDI0 · CHD5_HUMAN
- ProteinChromodomain-helicase-DNA-binding protein 5
- GeneCHD5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1954 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytosol | |
Cellular Component | heterochromatin | |
Cellular Component | membrane | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | NuRD complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | chromatin binding | |
Molecular Function | DNA binding | |
Molecular Function | H3K27me3 modified histone binding | |
Molecular Function | helicase activity | |
Molecular Function | histone binding | |
Molecular Function | metal ion binding | |
Biological Process | cerebral cortex neuron differentiation | |
Biological Process | chromatin remodeling | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of signal transduction by p53 class mediator | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | sperm DNA condensation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromodomain-helicase-DNA-binding protein 5
- EC number
- Short namesCHD-5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TDI0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Parenti-Mignot neurodevelopmental syndrome (PMNDS)
- Note
- DescriptionAn autosomal dominant neurodevelopmental disorder characterized by intellectual disability, speech delay, motor delay, behavioral problems, and epilepsy.
- See alsoMIM:619873
Natural variants in PMNDS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_087312 | 193 | R>Q | in PMNDS; dbSNP:rs1667056923 | |
VAR_087313 | 193 | R>W | in PMNDS; dbSNP:rs1571164162 | |
VAR_087314 | 272 | A>V | in PMNDS; uncertain significance; dbSNP:rs2100866749 | |
VAR_087315 | 314-1954 | missing | in PMNDS | |
VAR_087316 | 427 | E>K | in PMNDS; dbSNP:rs2100863089 | |
VAR_087317 | 596-1954 | missing | in PMNDS | |
VAR_087318 | 912 | S>F | in PMNDS; dbSNP:rs1474624774 | |
VAR_087319 | 1084 | D>N | in PMNDS; dbSNP:rs760743983 | |
VAR_087320 | 1124 | P>L | in PMNDS; dbSNP:rs2100847449 | |
VAR_087321 | 1136 | R>H | in PMNDS; dbSNP:rs1162494442 | |
VAR_087322 | 1140 | N>I | in PMNDS; dbSNP:rs2100846484 | |
VAR_087323 | 1419 | I>M | in PMNDS; dbSNP:rs371488822 | |
VAR_087324 | 1488 | D>V | in PMNDS; dbSNP:rs2100842233 | |
VAR_087325 | 1714 | E>G | in PMNDS |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035475 | 45 | in a breast cancer sample; somatic mutation; dbSNP:rs1470692239 | |||
Sequence: V → M | ||||||
Natural variant | VAR_035476 | 119 | in a breast cancer sample; somatic mutation; dbSNP:rs1667131228 | |||
Sequence: D → N | ||||||
Natural variant | VAR_087312 | 193 | in PMNDS; dbSNP:rs1667056923 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_087313 | 193 | in PMNDS; dbSNP:rs1571164162 | |||
Sequence: R → W | ||||||
Natural variant | VAR_087314 | 272 | in PMNDS; uncertain significance; dbSNP:rs2100866749 | |||
Sequence: A → V | ||||||
Natural variant | VAR_087315 | 314-1954 | in PMNDS | |||
Sequence: Missing | ||||||
Natural variant | VAR_087316 | 427 | in PMNDS; dbSNP:rs2100863089 | |||
Sequence: E → K | ||||||
Mutagenesis | 518 | Reduced affinity for trimethylated histone H3K27me3. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_087317 | 596-1954 | in PMNDS | |||
Sequence: Missing | ||||||
Mutagenesis | 619 | Reduced affinity for trimethylated histone H3K27me3. | ||||
Sequence: Y → E | ||||||
Natural variant | VAR_035477 | 667 | in a breast cancer sample; somatic mutation | |||
Sequence: R → G | ||||||
Natural variant | VAR_087318 | 912 | in PMNDS; dbSNP:rs1474624774 | |||
Sequence: S → F | ||||||
Natural variant | VAR_087319 | 1084 | in PMNDS; dbSNP:rs760743983 | |||
Sequence: D → N | ||||||
Natural variant | VAR_087320 | 1124 | in PMNDS; dbSNP:rs2100847449 | |||
Sequence: P → L | ||||||
Natural variant | VAR_087321 | 1136 | in PMNDS; dbSNP:rs1162494442 | |||
Sequence: R → H | ||||||
Natural variant | VAR_087322 | 1140 | in PMNDS; dbSNP:rs2100846484 | |||
Sequence: N → I | ||||||
Natural variant | VAR_048729 | 1253 | in dbSNP:rs6657997 | |||
Sequence: S → I | ||||||
Mutagenesis | 1390 | Abolishes methylation by N6AMT1. | ||||
Sequence: Q → R | ||||||
Natural variant | VAR_087323 | 1419 | in PMNDS; dbSNP:rs371488822 | |||
Sequence: I → M | ||||||
Natural variant | VAR_087324 | 1488 | in PMNDS; dbSNP:rs2100842233 | |||
Sequence: D → V | ||||||
Natural variant | VAR_048730 | 1539 | in dbSNP:rs2843493 | |||
Sequence: S → P | ||||||
Natural variant | VAR_087325 | 1714 | in PMNDS | |||
Sequence: E → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,754 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000080230 | 1-1954 | UniProt | Chromodomain-helicase-DNA-binding protein 5 | |||
Sequence: MRGPVGTEEELPRLFAEEMENEDEMSEEEDGGLEAFDDFFPVEPVSLPKKKKPKKLKENKCKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPNKKKKKKLKDKKEKKAKRKKKDEDEDDNDDGCLKEPKSSGQLMAEWGLDDVDYLFSEEDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTISPPLAVSPPQVPQPVPIRKAKTKEGKGPGVRKKIKGSKDGKKKGKGKKTAGLKFRFGGISNKRKKGSSSEEDEREESDFDSASIHSASVRSECSAALGKKSKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDDEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPDVEPSLPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELMLGEDTRLPKRLLKKGKKLRDDKQEKPPDTPIVDPTVKFDKQPWYIDSTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPVTPIPDVQSSKGGNLAASAKKKHGSTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLIPEGPEGKKSGEVISSDPNTPVPASPAHLLPAPLGLPDKMEAQLGYMDEKDPGAQKPRQPLEVQALPAALDRVESEDKHESPASKERAREERPEETEKAPPSPEQLPREEVLPEKEKILDKLELSLIHSRGDSSELRPDDTKAEEKEPIETQQNGDKEEDDEGKKEDKKGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYDIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEVHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQGAFGSSQMYSNNFGPNFRGPGPGGIVNYNQMPLGPYVTDI | |||||||
Modified residue (large scale data) | 558 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1390 | UniProt | N5-methylglutamine | ||||
Sequence: Q | |||||||
Modified residue | 1554 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1631 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Methylated at Gln-1390 by N6AMT1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Preferentially expressed in total brain, fetal brain, and cerebellum. It is also moderately expressed in the adrenal gland and detected in testis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the nucleosome remodeling and deacetylase (NuRD) repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5. The exact stoichiometry of the NuRD complex is unknown, and some subunits such as MBD2 and MBD3, GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive NuRD complexes. Interacts with HDAC2.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-134 | Disordered | ||||
Sequence: MRGPVGTEEELPRLFAEEMENEDEMSEEEDGGLEAFDDFFPVEPVSLPKKKKPKKLKENKCKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPNKKKKKKLKDKKEKKAKRKKKDEDEDDNDDGCLKEPKSS | ||||||
Compositional bias | 15-36 | Acidic residues | ||||
Sequence: FAEEMENEDEMSEEEDGGLEAF | ||||||
Compositional bias | 50-64 | Basic residues | ||||
Sequence: KKKPKKLKENKCKGK | ||||||
Compositional bias | 112-129 | Basic and acidic residues | ||||
Sequence: KRKKKDEDEDDNDDGCLK | ||||||
Region | 225-338 | Disordered | ||||
Sequence: PLAVSPPQVPQPVPIRKAKTKEGKGPGVRKKIKGSKDGKKKGKGKKTAGLKFRFGGISNKRKKGSSSEEDEREESDFDSASIHSASVRSECSAALGKKSKRRRKKKRIDDGDGY | ||||||
Compositional bias | 241-256 | Basic and acidic residues | ||||
Sequence: KAKTKEGKGPGVRKKI | ||||||
Compositional bias | 257-272 | Basic residues | ||||
Sequence: KGSKDGKKKGKGKKTA | ||||||
Zinc finger | 343-390 | PHD-type 1 | ||||
Sequence: QDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKE | ||||||
Region | 343-653 | Histone-binding | ||||
Sequence: QDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDDEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPDVEPSLPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELMLGEDT | ||||||
Zinc finger | 416-463 | PHD-type 2 | ||||
Sequence: MEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCP | ||||||
Domain | 497-554 | Chromo 1 | ||||
Sequence: LPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPF | ||||||
Region | 549-571 | Disordered | ||||
Sequence: DEPPPFDYGSGDEDGKSEKRKNK | ||||||
Domain | 592-653 | Chromo 2 | ||||
Sequence: MMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELMLGEDT | ||||||
Domain | 712-896 | Helicase ATP-binding | ||||
Sequence: RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPE | ||||||
Motif | 847-850 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 1028-1193 | Helicase C-terminal | ||||
Sequence: LLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDIL | ||||||
Region | 1209-1253 | Disordered | ||||
Sequence: MSQGQRPVTPIPDVQSSKGGNLAASAKKKHGSTPPGDNKDVEDSS | ||||||
Compositional bias | 1216-1230 | Polar residues | ||||
Sequence: VTPIPDVQSSKGGNL | ||||||
Region | 1351-1411 | Disordered | ||||
Sequence: YNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPL | ||||||
Compositional bias | 1386-1408 | Basic and acidic residues | ||||
Sequence: RPEGQSGRRQSRRQLKSDRDKPL | ||||||
Region | 1524-1564 | Disordered | ||||
Sequence: YSTPDLIPEGPEGKKSGEVISSDPNTPVPASPAHLLPAPLG | ||||||
Region | 1597-1640 | Disordered | ||||
Sequence: AALDRVESEDKHESPASKERAREERPEETEKAPPSPEQLPREEV | ||||||
Compositional bias | 1600-1640 | Basic and acidic residues | ||||
Sequence: DRVESEDKHESPASKERAREERPEETEKAPPSPEQLPREEV | ||||||
Region | 1658-1696 | Disordered | ||||
Sequence: SRGDSSELRPDDTKAEEKEPIETQQNGDKEEDDEGKKED |
Domain
The PHD domains mediate specific binding to histone H3 unmethylated at 'Lys-4' and may preferentially recruit the protein to transcriptionally inactive genes.
The chromo domains mediate specific binding to histone H3 trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron differentiation for proper gene regulation.
Sequence similarities
Belongs to the SNF2/RAD54 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,954
- Mass (Da)223,050
- Last updated2002-06-01 v1
- ChecksumE333062B5B55E71F
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 15-36 | Acidic residues | ||||
Sequence: FAEEMENEDEMSEEEDGGLEAF | ||||||
Compositional bias | 50-64 | Basic residues | ||||
Sequence: KKKPKKLKENKCKGK | ||||||
Compositional bias | 112-129 | Basic and acidic residues | ||||
Sequence: KRKKKDEDEDDNDDGCLK | ||||||
Compositional bias | 241-256 | Basic and acidic residues | ||||
Sequence: KAKTKEGKGPGVRKKI | ||||||
Compositional bias | 257-272 | Basic residues | ||||
Sequence: KGSKDGKKKGKGKKTA | ||||||
Compositional bias | 1216-1230 | Polar residues | ||||
Sequence: VTPIPDVQSSKGGNL | ||||||
Compositional bias | 1386-1408 | Basic and acidic residues | ||||
Sequence: RPEGQSGRRQSRRQLKSDRDKPL | ||||||
Compositional bias | 1600-1640 | Basic and acidic residues | ||||
Sequence: DRVESEDKHESPASKERAREERPEETEKAPPSPEQLPREEV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF425231 EMBL· GenBank· DDBJ | AAL98962.1 EMBL· GenBank· DDBJ | mRNA | ||
AL031847 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL035406 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL117491 EMBL· GenBank· DDBJ | CAB55959.1 EMBL· GenBank· DDBJ | mRNA | ||
AB007913 EMBL· GenBank· DDBJ | BAA32289.1 EMBL· GenBank· DDBJ | mRNA |